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PubMed2004

Evidence for a common pattern of peptidergic innervation of cnidocytes.

Tentacles from representatives of all four classes of the phylum Cnidaria were examined using antibodies against the neuropeptides FMRFamide and RFamide to reveal the organization of neurons and nerve nets associated with cnidocytes. The tentacles of all species examined contained FMRFamide- or RFamide-immunoreactive neurons, in varying densities. In representatives from the Scyphozoa, Hydrozoa, and Cubozoa, the FMRFamide-immunoreactive neurons formed plexuses at the base of the cnidocyte assemblages; in anthozoans, the absence of discrete assemblies of cnidocytes precluded visual co-localization of cnidocytes and immunoreactive neurons. In all four classes, immunoreactive sensory cells connected these peptidergic nerve nets to the surface of the tentacle. These findings suggest that members of all four cnidarian classes share a common organizational pattern, and it is proposed that this peptidergic innervation may be involved in the chemosensory regulation of cnidocyte discharge.

Animal Structures↗
PubMed1999

Differential processing of neuropeptides influences Drosophila heart rate.

Peptides that play critical physiological roles are often encoded in precursors that contain several structurally-related gene products. Differential processing of a precursor by cell-specific processing enzymes can yield multiple messengers with diverse distributions and activities. We have reported the isolation of SDNFMRFamide, DPKQDFMRFamide, and TPAEDFMRFamide from adult Drosophila melanogaster. The peptides are encoded in the FMRFamide gene and have a common C-terminal FMRFamide but different N-terminal extensions. In order to investigate the processing of the FMRFamide polypeptide protein precursor, we generated antisera to distinguish among the structurally-related neuropeptides. Utilizing a triple-label immunofluorescent protocol, we mapped the distribution of the peptides. Each peptide has a unique, non-overlapping cellular expression pattern in neural tissue suggesting that the precursor is differentially processed. In order to identify a biological activity of the peptides, we established an in vivo heart rate assay. SDNFMRFamide decreases heart rate but DPKQDFMRFamide and TPAEDFMRFamide do not, indicating that the N-terminal residues are critical for this activity. SDNFMRFamide immunoreactivity is present in the aorta, implying that SDNFMRFamide acts locally to affect heart rate; DPKQDFMRFamide and TPAEDFMRFamide antisera do not stain cardiac tissue. Our data support the conclusion that Drosophila contains cell-specific proteolytic enzymes to differentially process a polypeptide protein precursor resulting in unique expression patterns of structurally-related, yet functionally distinct neuropeptides.

Analysis of Variance↗
PubMed2000

Reorganization of peptidergic systems during brain regeneration in Eisenia fetida (Oligochaeta, Annelida).

After the extirpation of the brain reorganization of the peptidergic (FMRFamide, neuropeptide Y, proctolin) systems was studied in the newly forming cerebral ganglion of the annelid Eisenia fetida. During regeneration, all immunoreactive fibres appear on the 1st-2nd postoperative day. At the beginning of regeneration, immunoreactive neurons and fibres form a mixed structure in the wound tissue. On the 3rd postoperative day, FMRFamide positive and neuropeptide Y-immunoreactive, while on the 7th postoperative day proctolin-immunoreactive neurons appear in the loose wound tissue. From the 25th postoperative day a capsule gradually develops around it. The neurons of the preganglion move to the surface of the newly appearing preganglion. The number of these cells gradually increase, and by the 72th-80th postoperative days the localization and number of peptide-immunoreactive neurons is similar to that in the intact one. The neurons of all examined peptidergic systems may originate from the neuroblasts, situated on the inner and outer surface of the intact ganglia (e.g. suboesophageal and ventral cord ganglia). In addition FMRFamide and proctolin immunoreactive neurons may take their derive by mitotic proliferation from the pharyngeal neurons, too.

Animals↗
PubMedDate not supplied

Myotropic peptides in Drosophila melanogaster and the genes that encode them.

Myotropic peptides are structurally dissimilar; thus, they comprise different families. The cellular expressions of myotropins suggest they act as hormones, transmitters, and modulators of numerous biological processes. Drosophila melanogaster allatostatin (AST), FMRFamide-containing, dromyosuppressin (DMS), and drosulfakinin (DSK) peptides represent four different myotropin families. A different gene encodes each of these four myotropin families. D. melanogaster AST, FMRFamide-containing, DMS, and DSK peptides are present in neural and gut tissue, but are not all expressed in the same cells. These four families of myotropins affect spontaneous contractions of gut, heart, and/or reproductive tissue, but their effects are dissimilar in magnitude and time course. Based on their structures, genes, distributions, and activities, the synthesis and release of these D. melanogaster myotropins are likely governed by different sensory inputs and regulatory mechanisms. The differences in structures, precursors, cellular expressions, and activities are consistent with the conclusion that they do not play redundant roles in their effects on the frequency of muscle contractions. Orthologs of these D. melanogaster myotropins exist in other animal species; thus, research on the mechanisms involved in their production and processing, functions, and signaling may be widely applicable. Here, we review research on D. melanogaster AST, FMRFamide-containing, myosuppressin, and sulfakinin peptides.

Animals↗
PubMed2002

Peripheral nerve connections influence the appearance of neurosecretary material in neural sheath of ventral ganglion of the fly Sarcophaga bullata: an immunocytochemical study.

This study examined the role of the brain and peripheral connections with the target organs in the appearance of neurosecretary material within the dorsal neural sheath of the ventral ganglion of the fly S. bullata. Specifically, the accumulation of the neuropeptide FMRFamide (the neurosecretary material) was examined by immunocytochemistry. Immunoreactions were performed on: (1) a normal intact ventral ganglion, (2) an isolated ventral ganglion that was cultured in vivo, and (3) a ventral ganglion that was isolated by transection from the brain, but retained its peripheral nerve connections. The results demonstrate that (a) the neurons of the ganglia survive and exhibit FMRFamide immune reaction independent of their peripheral connections, and (b) the accumulation of neuropeptide in the dorsal neural sheath is controlled by intact peripheral nerve connections with the ganglion. It is suggested that in the absence of their peripheral connections, the axons of FMRFamide immunoreactive neurons fail to invade the neural sheath resulting in the accumulation of neurosecretary material.

Animals↗
PubMedDate not supplied

Various signal molecules modulate voltage-activated ion currents on snail neurons.

The modulatory effects of interleukin-1 (IL-1), an immunotransmitter, and FMRFamide, a molluscan neuropeptide, were studied on identified neurons of Helix pomatia L. (Mollusca, Gastropoda) by using the method of two microelectrode voltage clamp. IL-1 and FMRFamide uniformly decreased the voltage-activated inward current (ICa), while the voltage-dependent outward potassium current (Inet K) increased. IL-1 and FMRFamide were shown to use the same cellular targets as used by the low molecular weight neurotransmitters.

Animals↗
PubMed1990

Effect of Phe-D-Met-Arg-Phe-NH2 and other Phe-Met-Arg-Phe-NH2-related peptides on mouse colonic propulsive motility: a structure-activity relationship study.

The effect of several i.c.v.-administered FMRFamide (Phe-Met-Arg-Phe-NH2)-like peptides (FaRPs) on mouse colonic propulsive motility was examined. Dose-related inhibition of propulsive motility (measured as an increase in the time of colonic bead expulsion) was produced by analogs with either the sequence (-)F[X]RFamide or with the FMRFamide sequence containing D-amino acid substitutions. The C-terminal dipeptide sequence Arg-Phe-NH2 was sufficient to produce this effect. D-amino acid substitution in the second position, i.e., [D-Met2]-FMRFamide (DMFa), conferred significantly enhanced activity (nearly maximal obtainable response under the test conditions) in this preparation (ED25 = 2.3 micrograms = 3.8 nmol). DMFa did not block the action of morphine but, like morphine, was blocked by the opioid antagonist naloxone and was attenuated by 24-hr pretreatment with the selective mu-1 opioid antagonist naloxonazine (35 mg/kg s.c.). It is concluded that a variety of FaRPs, particularly those with a nonpolar residue in the first position and with Arg in the third position, behave as opioid-like agonists, not antagonists, on mouse colonic propulsive motility. DMFa is identified as the most active FaRP studied to date on this endpoint.

Animals↗
PubMed1990

Occurrence and distribution of putative neurotransmitters in the frog-lung parasite Haplometra cylindracea (Trematoda: Digenea).

The localisation and distribution of the cholinergic, serotoninergic and peptidergic components of the nervous system of the frog-lung fluke Haplometra cylindracea have been determined by the application of standard enzyme cytochemical and immunocytochemical techniques to cryostat sections and whole-mount preparations. Cholinesterase activity (ChE), as indicative of acetylcholine, has been demonstrated cytochemically in the CNS and PNS; however, the anterior ganglia were notably unreactive. The occurrence of serotonin was examined by an indirect immunofluorescence technique, and immunoreactivity (IR) was demonstrable in small, paired anterior ganglia and in fine nerve fibres associated with the somatic muscle, cirrus and gonopore. The peptidergic portion of the nervous system was investigated using antisera to 17 mammalian regulatory peptides and the invertebrate peptide FMRFamide, and was visualised by both indirect immunofluorescence and confocal scanning laser microscopy. Positive immunostaining occurred with antisera raised against pancreatic polypeptide (PP), peptide tyrosine tyrosine (PYY), substance P (SP), peptide histidine isoleucine (PHI) and FMRFamide. Immunoreactivity to PP, PYY and FMRFamide was widespread throughout the nervous system and was evident in large, paired anterior ganglia, the dorsal commissure, main nerve tracts and the extensive array of small fibres that constitute the PNS. In contrast, the distribution of nerves immunoreactive to SP and PHI was less apparent, with PHI-IR occurring exclusively within the fibrous neuropile of the ganglia and in fibres of the ventral nerve cord. Results are discussed with respect to the distribution of the various neurochemical elements and their roles as putative neurotransmitters and/or regulatory molecules.

Animals↗
PubMed1994

Serotonin and neuropeptide immunoreactivities in the intramolluscan stages of three marine trematode parasites.

Using an indirect immunofluorescence technique interfaced with confocal scanning laser microscopy, whole-mount preparations of three genera of marine trematode larvae, Cryptocotyle lingua, Cercaria emasculans and Himasthla leptosoma, were screened for 5-hydroxytryptamine (5-HT) and selected neuropeptide immunoreactivities (IRs). IRs for pancreatic polypeptide (PP), peptide YY (PYY) and FMRFamide were found in the central nervous systems of the three species of cercariae, immunostaining the paired ganglia and central commissure and the longitudinal nerve cords, with slight differences in both distribution and intensity of IRs being observed for the different antisera used. PP, PYY and FMRFamide IRs were evident in both central and peripheral components of the nervous system in the rediae of C. lingua. 5-HT IR was confined to the peripheral nervous systems of the cercariae of C. emasculans and the rediae of C. lingua, appearing in the form of a network of immunoreactive fibres and associated large cell bodies. A moderate substance P IR was observed in the nervous system of the cercariae of C. lingua. The patterns of immunostaining described were compared with those obtained using antiserum directed to the C-terminal decapeptide amide of neuropeptide F (NPF), a native parasitic peptide from the cestode Moniezia expansa. Results demonstrated that serotoninergic and peptidergic components were present in the nervous systems of all of the trematode larvae studied and that some, if not all, of the IR for PP, PYY and FMRFamide was due to the presence of a trematode NPF homologue.

Amino Acid Sequence↗
PubMed2003

Comparative potency of some extended peptide chain members of the RFamide neuropeptide family, assessed on the hearts of Busycon canaliculatum and Buccinum undatum.

Twenty different RFamide neuropeptide analogues were examined for their relative potencies on the ventricles of Busycon canaliculatum and Buccinum undatum and on the atrium of Busycon to determine the essential requirements for activity at the RFamide receptor. None of the neuropeptide studies was inhibitory to natural cardiac rhythmicity or to FMRFamide (Phe-Met-Arg-Phe-NH(2)) or FLRFamide (Phe-Leu-Arg-Phe-NH(2)) responses. Two tripeptides studied were completely without effect, indicating that a minimum of four amino acids in the peptide chain length was essential for any activity. The original parent tetrapeptide FMRFamide was surprisingly less potent than many of the extended chain peptides such as the penta, hepta and decapeptides. These RFamide neuropeptides were strongly inotropic on both ventricles and the atrium, while on the latter they were strongly chronotropic despite several of these peptides being of a non-molluscan origin. Chain length seems to be of little importance for activity at the receptor. Surprisingly, SCP(B) (small cardioactive Peptide B) was not very effective in either Busycon or Buccinum ventricle. What was also clear was that the configuration of the carboxyl terminal was important for activity. Two neuropeptides in this study possessed an Arg-Met carboxyl terminal and were much less effective than FMRFamide, suggesting that an Arg-Phe terminal is most effective in receptor activation.

Amino Acid Sequence↗
PubMed2005

Neurochemical characterization of nervous elements innervating the body wall of earthworms (Lumbricus, Eisenia): immunohistochemical and pharmacological studies.

The distribution and chemical neuroanatomy of nervous elements and certain pharmacological-physiological characteristics of the innervation of the body wall in earthworms are described. Solitary sensory bipolar cells can be found among the epithelial cells. These bipolar cells contain serotonin, tyrosine hydroxylase, histamine, gamma-amino-butyric acid (GABA), Eisenia tetradecapeptide, proctolin or rhodopsin in various combinations. In the body wall, the plexus sub-muscularis is composed of nerve fibres only, whereas the plexus sub-epithelialis and muscularis also contain solitary nerve cells. These cells display histamine, GABA or neuropeptide Y immunoreactivity. The fibres of the three plexuses are reactive to serotonin, histamine, Eisenia tetradecapeptide, proctolin, GABA and neuropeptide Y antibodies. FMRFamide-immunoreactive fibres of the plexus muscularis originate from the central nervous system, whereas axons containing the other studied molecules are derived from both peripheral and central structures. High pressure liquid chromatography assays have revealed serotonin, dopamine and histamine in the body wall. Contractions of the body wall musculature can be elicited with serotonin and FMRFamide. Serotonin-evoked contractions are suppressed by the application of GABA. Serotonin acts both directly on the muscle cell receptors and indirectly through initiating transmitter release from the nervous elements, whereas the FMRFamide-induced contractions seem to be mediated through the muscle cell receptors only. The pharmacological profiles of the serotonin and GABA receptors resemble those of the vertebrate 5-HT(3) and GABA(B) receptor types. Our findings indicate that both the sensory and efferent system of the annelid body wall operate by means of a variety of neuroactive compounds, suggesting a complex role of signalling systems in the regulation of this organ.

Animals↗
PubMed1994

Biological activity and receptor binding properties of some analogues of pQDPFLRFamide.

To investigate the role of the N-terminal region of the heptapeptide FMRFamide-like peptide, pQDPFLRFamide, three analogues were synthesized. The analogues [pQNPFLRFamide, pQDAibFLRFamide (Aib = aminoisobutyric acid) and pQDGFLRFamide] contained modifications at amino acid residues 2 and 3, which we believed might be critical for maintaining the bioactive conformation of the heptapeptide. The analogues were tested for their ability to bind to receptors in membranes from Helix aspersa circumoesophageal ganglia and for their biological effects on the isolated Helix heart, the Helix tentacle retractor muscle, and extensor-tibiae neuromuscular preparation of the locust. Schistocerca gregaria. The substitution of Asn for Asp2 and that of Aib for Pro3 were conservative with respect to retention of heptapeptide-like biological activity, whereas the substitution of Gly for Pro3 significantly improved the binding affinity of the peptide for the FMRFamide receptors and conferred on the peptide some characteristic FMRFamide-like biological activity. Thus, pQDPFLRFamide bioactivity may depend on a bent conformation in solution.

Amino Acid Sequence↗
PubMed1995

Suppressing effects of neuroactive peptides on the inward current caused by achatin-I, an Achatina endogenous peptide.

1. Modulatory effects of the four molluscan neuroactive peptides. FMRFamide (Phe-Met-Arg-Phe-NH2), APGW-amide (Ala-Pro-Gly-Trp-NH2), oxytocin and [SER2]-Mytilus inhibitory peptide ([SER2]-MIP) (Gly-Ser-Pro-Met-Phe-Val-NH2) were examined on the inward current (Iin) caused by achatin-I (Gly-D-Phe-Ala-Asp), which has been isolated from the Achatina ganglia. 2. Two Achatina giant neurone types, v-RCDN (ventral-right cerebral distinct neurone) and PON (periodically oscillating neurone), were used. Achatin-I was applied locally to the neurone tested by brief pneumatic pressure ejection, and the other molluscan neuroactive peptides were perfused around the ganglia. 3. FMRFamide, perfused at 3 microM, suppressed markedly the Iin elicited by the achatin-I of both v-RCDN and PON. APGW-amide at 3 microM also suppressed the Iin of v-RCDN, but did not affect that of PON. Oxytocin at 1 microM suppressed the Iin of PON, but did not affect that of v-RCDN. [Ser2]-MIP at 3 microM did not affect the Iin of v-RCDN. 4. The dose-response curves of FMRFamide, APGW-amide and oxytocin, indicated that their respective suppressive effects on the Iin of achatin-I were dose-dependent, and that APGW-amide was slightly more potent than the other peptides. The dose (pressure duration)-response curves of achatin-I (1 kg/cm2, 10(-3) M, 5 min interval), obtained by varying the duration of the achatin-I pressure ejection, were measured in the presence and absence of each of the three peptides.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1994

Presynaptic mechanisms regulating Ca2+ concentration triggering acetylcholine release at an identified neuro-neuronal synapse of Aplysia.

We have used an identified cholinergic neuro-neuronal synapse in the buccal ganglion of Aplysia to determine which types of Ca2+ channels are involved in triggering transmitter release. omega-Conotoxin as well as funnel web spider toxin partially reduced acetylcholine release indicating that both N- and P-type Ca2+ channels are involved. Nifedipine-sensitive L-type Ca2+ channels are also present but they are not directly implicated in acetylcholine release. We have identified presynaptic receptors to two peptides. FMRFamide and buccalin and to the neurotransmitter histamine. FMRFamide facilitates acetylcholine release by increasing the presynaptic Ca2+ influx whereas buccalin and histamine have an opposite effect. These neuromodulators control only the influx of Ca2+ through N-type Ca2+ channels since their action on transmitter release can be prevented by omega-conotoxin but not by funnel web spider toxin. FMRFamide and histamine, respectively, increased and decreased Ca2+ influx by shifting in opposite ways the voltage sensitivity to activation of the channels. Buccalin reduced Ca2+ influx by decreasing the number of available channels. 2,5-Diterbutyl 1,4-benzohydroquinone, a blocker of the reticulum Ca2+ pump, increased evoked transmitter release by increasing the intracellular concentration of Ca2+ without affecting the presynaptic Ca2+ influx. It is suggested that a reticulum-like Ca2+ buffer, in close proximity to N- and P-type Ca2+ channels, controls the intracellular concentrations of Ca2+ actually triggering acetylcholine release.

Acetylcholine↗
PubMed1987

Effects of synthetic peptides on giant neurones identified in the ganglia of an African giant snail (Achatina fulica Férussac). IV.

1. The previous papers (Ku et al., 1986; Kim et al., 1987; Yongsiri et al., 1987) reported the effects of the synthetic peptides, i.e. Met-enkephalin, substance P, neurotensin, oxytocin, Arg-vasopressin, proctolin, FMRFamide, ranatensin C etc., on about 20 identifiable giant neurones of an African giant snail (Achatina fulica Férussac). 2. In the present study, the effects of the same peptides on the following Achatina neurones, other than those of the previous papers, were investigated: v-RPLN, v-LPSN, v-VNAN, v-VLN, r-VMN, l-VMN, v-l-VOrN and d-RCDN. 3. Of the neurones tested here, v-RPLN (ventral-right parietal large neurone) was excited slightly by Met-enkephalin, excited markedly by oxytocin, and inhibited by FMRFamide, at 10(-4) M. 4. Of these effects, those of oxytocin and FMRFamide were undoubtedly the direct effects on the neurone tested, whereas those of Met-enkephalin were probably due to the synaptic activations. 5. Another neurone, v-LPSN (ventral-left parietal large neurone), was affected by oxytocin and ranatensin C at 10(-4) M. The two substances sometimes showed similar simple excitatory effects, in other cases biphasic (excitation followed by inhibition) effects, and in a few cases almost no effect. 6. The rest of the neurones tested were not sensitive at all to any of the peptides examined.

Animals↗
PubMed1998

Monogenean neuromusculature: some structural and functional correlates.

Monogenean neuromuscular systems are structurally and functionally well-differentiated, as evidenced by research on the fish-gill parasite, Diclidophora merlangi. The nervous system in the worm exhibits a raft of putative intercellular signalling molecules, localised in neuronal vesicles. There is cytochemical evidence of co-localisation of neuropeptides and cholinergic substances, with aminergic components generally occupying separate neurons. The phalloidin-fluorescence technique for F-actin has enabled the demonstration of muscle organisation in the worm. Body wall musculature comprises circular, longitudinal and diagonal arrays of myofibres whose contractions are believed to be largely myogenic; circular fibres predominate in the walls of the reproductive tracts. The major somatic muscles are longitudinal muscle bundles that traverse the mesenchyme, the most extensive of which extend from the pharynx to the clamps of the haptor. Experiments have shown that some of these muscles may serve in a withdrawal reflex in the worm, which can be evoked by water turbulence. These and the muscles of the suckers, pharynx, clamps, male copulatory organ and ootype are provided with extensive synaptic innervation that is strongly immunoreactive for FMRFamide-related peptides (FaRPs), suggesting contractions may be neurogenic. Examination of the physiological effects of known flatworm FMRFamide-related peptides on muscle contractility in vitro has shown those FMRFamide-related peptides isolated from turbellarians to be the most excitatory. Results are discussed with respect to neuromuscular function in adhesion, alimentation, and reproduction in the worm.

Animals↗
PubMed2003

Effects of neuropeptide SF and related peptides on acid sensing ion channel 3 and sensory neuron excitability.

Acid sensing ion channel 3 (ASIC3) is a cation channel gated by extracellular protons. It is highly expressed in sensory neurons, including small nociceptive neurons and has been proposed to participate in pain perception associated with tissue acidosis and in mechanoperception. Neuropeptide FF (NPFF) and FMRFamide have been shown to potentiate proton-gated currents from cultured sensory neurons and acid sensing ion channel (ASIC) cDNA transfected cells. In this study, we report that another mammalian peptide neuropeptide SF (NPSF), derived from the same precursor, also considerably increases the amplitude of the sustained current of heterologously expressed ASIC3 (12-fold vs. 19- and nine-fold for FMRFamide and NPFF, respectively) with an EC(50) of approximately 50 microM. Similar effects were also observed on endogenous ASIC3-like sustained current recorded from DRG neurons although of smaller amplitudes (two-, three- and seven-fold increase for NPSF, NPFF and FMRFamide, respectively), and essentially related to a slowing down of the inactivation rate. Importantly, this modulation induced changes in neuronal excitability in response to an electrical stimulus applied during extracellular acidification. ASIC3-mediated sustained depolarisation, and its regulation by neuropeptides, could thus be important in regulating polymodal neuron excitability particularly under inflammatory conditions where the expression levels of both NPFF precursor and ASIC3 are increased.

Acid Sensing Ion Channels↗
PubMed1996

Characterization of the gene for leucomyosuppressin and its expression in the brain of the cockroach Diploptera punctata.

Using HPLC separation, radioimmunoassay, and subsequent bioassay, we have detected the presence of an active peptide, which co-elutes with the insect myoinhibitory peptide leuco-myosuppressin, in the brain of the cockroach Diploptera punctata. We have isolated a cDNA encoding the precursor for this peptide from cDNA libraries representing D. punctata brain RNA. The cDNA sequence contains an open reading frame that upon translation would result in a prepropolypeptide of 96 amino acids. Proteolytic cleavage of the predicted precursor could result in several peptides, including a 10 amino acid C-terminal peptide that would, upon modification of the NH2 and COOH-terminal amino acids, be identical to the insect FLRFamide, leucomyosuppressin. No other RFamide products are predicted to be processed from the precursor. Southern blot analysis indicates that the gene is present in the D. punctata genome in a single copy. Northern blot analysis shows that the gene is predominantly expressed as a 3.8 kb mRNA in cockroach brain. Study of the expression of the leucomyosuppressin gene in D. punctata brain, using in situ hybridization, indicates that expression occurs primarily in the pars intercerebralis of the protocerebrum, a region showing abundant FMRFamide-like immunoreactive neurosecretory cells. Immunohistochemistry and HPLC coupled to radioimmunoassay indicates that leucomyosuppressin represents a significant proportion of FMRFamide-related peptide production in the brain. However, HPLC analysis also indicates the presence of significant levels of other related peptides, demonstrating the presence of more than one FMRFamide-related gene in this insect.

Amino Acid Sequence↗